L0777
Lipase from Aspergillus oryzae
solution, ≥100,000 U/g, white, beige
Synonym(s):
AOL, Lipolase 100L
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About This Item
CAS Number:
Enzyme Commission number:
3.1.1.3.
EC Number:
MDL number:
UNSPSC Code:
12352204
NACRES:
NA.54
Recommended Products
biological source
Aspergillus sp. (Aspergillus oryzae)
Quality Level
form
solution
specific activity
≥100,000 U/g
storage condition
(Tightly closed. Dry)
technique(s)
cell based assay: suitable
color
beige
white
storage temp.
2-8°C
InChI
1S/C11H9N3O2.Na/c15-8-4-5-9(10(16)7-8)13-14-11-3-1-2-6-12-11;/h1-7,16H,(H,12,14);/q;+1/b13-9-;
InChI key
QWZUIMCIEOCSJF-CHHCPSLASA-N
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General description
Research area: Cell Signaling
Lipase is derived from Aspergillus oryzae by ammonium sulfate precipitation and chromatography.Lipases or triacylglycerol acyl hydrolases are a group of hydrolase enzymes that are usually found in humans and animals with monogastric stomachs. Lipase enzymes are generally formed in the pancreas and stomach where they aid in fat and lipids digestion.(2)
Lipase is derived from Aspergillus oryzae by ammonium sulfate precipitation and chromatography.Lipases or triacylglycerol acyl hydrolases are a group of hydrolase enzymes that are usually found in humans and animals with monogastric stomachs. Lipase enzymes are generally formed in the pancreas and stomach where they aid in fat and lipids digestion.(2)
Application
Lipase from Aspergillus oryzae has been used:
- as a control enzyme in activity assays
- as a component in lipolase stock solution for the hydrolysis experiments
- to incubate scaffolds for lipase-accelerated degradation experiments
- as the lipolytic enzyme standard to detect lipolytic enzymatic activity via chromogenic agar plates and zymography
Biochem/physiol Actions
Lipase is widely used in several industries including food and pharmaceuticals. It mediates the hydrolysis of fats and oil. Lipase is utilized for peptide synthesis and in the detergent industry. It is active in the range of pH 2-5 and temperature between 30-50°C. Metal ions such as Fe2+, Fe3+, and Cu2+ prevent the action of lipase. A less polar organic solvent is preferred for high stability.Lipases play a crucial role in digestion as well as the transportation and processing of dietary lipid substrates by catalyzing the hydrolysis of ester bonds in lipid substrates. The lipase from Aspergillus oryzae (AOL), a multipurpose biocatalyst can be used in the kinetic resolution of a biotin intermediate lactone,α-lipoic acid, and 1-phenylethanol. Additionally, it has the ability to stereoselectively catalyze the hydrolysis of ethyl 2-(4-hydroxyphenoxy) propanoate and its analogs, which are key intermediates in the production of aryloxyphenoxypropionate herbicides. AOL serves as a promising biocatalyst in the esterification of a series of short-chain acids and alcohols to produce flavor esters. It can be used to catalyze the esterification of lauric acid with aromatic alcohol-benzyl alcohol.
Preparation Note
Produced by submerged fermentation of a genetically modified Aspergillus oryzae microorganism
Legal Information
A product of Novozyme Corp.
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Signal Word
Danger
Hazard Statements
Precautionary Statements
Hazard Classifications
Resp. Sens. 1
Storage Class Code
11 - Combustible Solids
WGK
WGK 1
Flash Point(F)
Not applicable
Flash Point(C)
Not applicable
Personal Protective Equipment
dust mask type N95 (US), Eyeshields, Gloves
Certificates of Analysis (COA)
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Hong De Yan et al.
3 Biotech, 9(7), 265-265 (2019-06-21)
The lipase from Aspergillus oryzae was modified with a surfactant and then observed to exhibit high catalytic efficiency and enantioselectivity for the kinetic resolution of (RS)-1-phenylethanol. The influential factors of the modified-lipase preparation were investigated, including the surfactant source, the
E E van Haaften et al.
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Cech J, et al.
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E E van Haaften et al.
Acta biomaterialia, 92, 48-59 (2019-05-21)
To maintain functionality during in situ vascular regeneration, the rate of implant degradation should be closely balanced by neo-tissue formation. It is unknown, however, how the implant's functionality is affected by the degradation of the polymers it is composed of.
Lipolase catalyzed synthesis of benzyl esters of fatty acids
Shintre MS, et al.
Biochemical Engineering Journal, 12, 131-141 (2002)
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